QRT3_ARATH
ID QRT3_ARATH Reviewed; 481 AA.
AC O49432;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Polygalacturonase QRT3;
DE Short=AtQRT3;
DE Short=PG QRT3;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase QRT3;
DE AltName: Full=Protein QUARTET 3;
DE Flags: Precursor;
GN Name=QRT3; OrderedLocusNames=At4g20050; ORFNames=F18F4.150;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=14551328; DOI=10.1104/pp.103.028266;
RA Rhee S.Y., Osborne E., Poindexter P.D., Somerville C.R.;
RT "Microspore separation in the quartet 3 mutants of Arabidopsis is impaired
RT by a defect in a developmentally regulated polygalacturonase required for
RT pollen mother cell wall degradation.";
RL Plant Physiol. 133:1170-1180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: Polygalacturonase required for degrading the pollen mother
CC cell wall during microspore development. {ECO:0000269|PubMed:14551328}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-
CC galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:14551328}.
CC -!- TISSUE SPECIFICITY: Expressed in the tapetum cells in the anthers and
CC in the ovules of open flowers. {ECO:0000269|PubMed:14551328}.
CC -!- DEVELOPMENTAL STAGE: Transiently expressed during the early microspore
CC stage. {ECO:0000269|PubMed:14551328}.
CC -!- DISRUPTION PHENOTYPE: The mature pollen grains are arranged in a
CC tetrad. A layer of material is frequently deposited on the surface of
CC the distal region of the pollen grains. {ECO:0000269|PubMed:14551328}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; AY268942; AAQ83300.1; -; mRNA.
DR EMBL; AY268941; AAQ83299.1; -; Genomic_DNA.
DR EMBL; AL021637; CAA16613.1; -; Genomic_DNA.
DR EMBL; AL161552; CAB79005.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84266.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84267.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67839.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67840.1; -; Genomic_DNA.
DR PIR; T04889; T04889.
DR RefSeq; NP_001078410.1; NM_001084941.2.
DR RefSeq; NP_001329640.1; NM_001341396.1.
DR RefSeq; NP_001329641.1; NM_001341397.1.
DR RefSeq; NP_193738.1; NM_118124.3.
DR AlphaFoldDB; O49432; -.
DR SMR; O49432; -.
DR STRING; 3702.AT4G20050.1; -.
DR PaxDb; O49432; -.
DR PRIDE; O49432; -.
DR ProteomicsDB; 226091; -.
DR EnsemblPlants; AT4G20050.1; AT4G20050.1; AT4G20050.
DR EnsemblPlants; AT4G20050.2; AT4G20050.2; AT4G20050.
DR EnsemblPlants; AT4G20050.6; AT4G20050.6; AT4G20050.
DR EnsemblPlants; AT4G20050.7; AT4G20050.7; AT4G20050.
DR GeneID; 827750; -.
DR Gramene; AT4G20050.1; AT4G20050.1; AT4G20050.
DR Gramene; AT4G20050.2; AT4G20050.2; AT4G20050.
DR Gramene; AT4G20050.6; AT4G20050.6; AT4G20050.
DR Gramene; AT4G20050.7; AT4G20050.7; AT4G20050.
DR KEGG; ath:AT4G20050; -.
DR Araport; AT4G20050; -.
DR TAIR; locus:2119832; AT4G20050.
DR eggNOG; ENOG502QV3U; Eukaryota.
DR HOGENOM; CLU_031155_0_0_1; -.
DR InParanoid; O49432; -.
DR PhylomeDB; O49432; -.
DR BioCyc; ARA:AT4G20050-MON; -.
DR PRO; PR:O49432; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49432; baseline and differential.
DR Genevisible; O49432; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004650; F:polygalacturonase activity; IDA:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009556; P:microsporogenesis; IMP:TAIR.
DR GO; GO:0010584; P:pollen exine formation; IMP:TAIR.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR039279; QRT3-like.
DR PANTHER; PTHR33928; PTHR33928; 1.
DR Pfam; PF12708; Pectate_lyase_3; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 2: Evidence at transcript level;
KW Cell wall; Cell wall biogenesis/degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..481
FT /note="Polygalacturonase QRT3"
FT /id="PRO_0000370639"
FT REPEAT 203..226
FT /note="PbH1 1"
FT REPEAT 261..282
FT /note="PbH1 2"
FT REPEAT 356..377
FT /note="PbH1 3"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 481 AA; 51659 MW; 9299F16297364257 CRC64;
MELRKSQVAM PVFLAIMSLM VSQVVFAEKD SGSMSPHDRA LAEMQALKAS LVRRNLPALV
SPPPTPPQAV PGPRVYQVIS YGADPTGKLD STDAILKAME EAFDGPNHGV LMQGINDLGG
ARIDLQGGSY LISRPLRFPS AGAGNLLISG GTLRASNDFP VDRYLIELKD ESSKLQYIFE
YITLRDLLID CNYRGGAIAV INSLRTSIDN CYITRFGDTN GILVKSGHET YIRNSFLGQH
ITAGGDRGER SFSGTAINLM GNDNAVTDTV IFSARIGVMV SGQANLLSGV HCYNKATGFG
GTGIYLRLPG LTQNRIVNSY LDYTGIVAED PVQLQISGTF FLGDAFILLK SIAGYIRGVS
IVDNMFSGSG HGVQIVQLDQ RNTAFDDVGQ VVVDRNSVNG MVEKSTVARG SVDGNGTSWT
VDFNPVLLFP DLINHVQYTL VASEAGVFPL HALRNVSDNR VVVETNAPVT GTVYVTVNQG
V
